Linked Life Data

17996313

Source:http://linkedlifedata.com/resource/pubmed/id/17996313

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2007-12-10
pubmed:abstractText
Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, as reported for most kelch-containing proteins. Here we showed that alpha-enolase and MBP-1 associate with NS1-BP in vitro and in vivo by GST pull-down assays and coimmunoprecipitation experiments; subsequent immunofluorescent staining confirmed colocalization of the proteins within the cells. Furthermore, functional analyses performed by cotransfection assays revealed that NS1-BP enhances the inhibitory effect exerted by MBP-1 on c-Myc promoter. In mammalian cells, the overexpression of both proteins resulted in an increased repression of basal c-Myc transcription and consistently affected the steady state levels of endogenous c-Myc mRNA. These findings further support the distinct roles of alpha-enolase and its MBP-1 variant in maintaining cell homeostasis. Moreover, our data suggest a novel function for NS1-BP in the control of cell proliferation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1773
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1774-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17996313-Actins, pubmed-meshheading:17996313-Animals, pubmed-meshheading:17996313-COS Cells, pubmed-meshheading:17996313-Cercopithecus aethiops, pubmed-meshheading:17996313-DNA-Binding Proteins, pubmed-meshheading:17996313-Gene Expression Regulation, pubmed-meshheading:17996313-HeLa Cells, pubmed-meshheading:17996313-Humans, pubmed-meshheading:17996313-Nuclear Proteins, pubmed-meshheading:17996313-Phosphopyruvate Hydratase, pubmed-meshheading:17996313-Promoter Regions, Genetic, pubmed-meshheading:17996313-Protein Binding, pubmed-meshheading:17996313-Protein Transport, pubmed-meshheading:17996313-Proto-Oncogene Proteins c-myc, pubmed-meshheading:17996313-Subcellular Fractions, pubmed-meshheading:17996313-Transcription, Genetic, pubmed-meshheading:17996313-Transcription Factors, pubmed-meshheading:17996313-Tumor Markers, Biological, pubmed-meshheading:17996313-Tumor Suppressor Proteins
pubmed:year
2007
pubmed:articleTitle
The kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control.
pubmed:affiliation
Dipartimento di Oncologia Sperimentale e Applicazioni Cliniche, Università di Palermo, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't